2odj
From Proteopedia
Crystal structure of the outer membrane protein OprD from Pseudomonas aeruginosa
Structural highlights
FunctionPORD_PSEAE Porin with a specificity for basic amino acids. Also possesses serine protease activity.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedOprD proteins form a large family of substrate-specific outer-membrane channels in Gram-negative bacteria. We report here the X-ray crystal structure of OprD from Pseudomonas aeruginosa, which reveals a monomeric 18-stranded beta-barrel characterized by a very narrow pore constriction, with a positively charged basic ladder on one side and an electronegative pocket on the other side. The location of highly conserved residues in OprD suggests that the structure represents the general architecture of OprD channels. Structural insight into OprD substrate specificity.,Biswas S, Mohammad MM, Patel DR, Movileanu L, van den Berg B Nat Struct Mol Biol. 2007 Nov;14(11):1108-9. Epub 2007 Oct 21. PMID:17952093[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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